ERG3_CANGA
ID ERG3_CANGA Reviewed; 364 AA.
AC P50860;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Delta(7)-sterol 5(6)-desaturase;
DE EC=1.14.19.20;
DE AltName: Full=C-5 sterol desaturase;
DE AltName: Full=Ergosterol Delta(5,6) desaturase;
DE AltName: Full=Sterol-C5-desaturase;
GN Name=ERG3; OrderedLocusNames=CAGL0F01793g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2001-L5;
RX PubMed=8593007; DOI=10.1128/aac.39.12.2708;
RA Geber A., Hitchcock C.A., Swartz J.E., Pullen F.S., Marsden K.E.,
RA Kwon-Chung K.J., Bennett J.E.;
RT "Deletion of the Candida glabrata ERG3 and ERG11 genes: effect on cell
RT viability, cell growth, sterol composition, and antifungal
RT susceptibility.";
RL Antimicrob. Agents Chemother. 39:2708-2717(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the introduction of a C-5 double bond in the B ring
CC of ergosterol. May contribute to the regulation of ergosterol
CC biosynthesis. {ECO:0000250|UniProtKB:P32353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:54320, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:138130,
CC ChEBI:CHEBI:138131; EC=1.14.19.20;
CC Evidence={ECO:0000250|UniProtKB:P32353};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from
CC zymosterol: step 3/5.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L40390; AAB02330.1; -; Genomic_DNA.
DR EMBL; CR380952; CAG58974.1; -; Genomic_DNA.
DR RefSeq; XP_446050.1; XM_446050.1.
DR AlphaFoldDB; P50860; -.
DR STRING; 5478.XP_446050.1; -.
DR EnsemblFungi; CAG58974; CAG58974; CAGL0F01793g.
DR GeneID; 2887958; -.
DR KEGG; cgr:CAGL0F01793g; -.
DR CGD; CAL0129591; ERG3.
DR VEuPathDB; FungiDB:CAGL0F01793g; -.
DR eggNOG; KOG0872; Eukaryota.
DR HOGENOM; CLU_047036_3_0_1; -.
DR InParanoid; P50860; -.
DR OMA; IFPLQKM; -.
DR UniPathway; UPA00768; UER00762.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000248; F:C-5 sterol desaturase activity; IEA:EnsemblFungi.
DR GO; GO:0050046; F:delta7-sterol 5(6)-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:CGD.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..364
FT /note="Delta(7)-sterol 5(6)-desaturase"
FT /id="PRO_0000117022"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 188..312
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 201..205
FT /note="Histidine box-1"
FT MOTIF 214..218
FT /note="Histidine box-2"
FT MOTIF 289..293
FT /note="Histidine box-3"
SQ SEQUENCE 364 AA; 42735 MW; 91010FD86BC137F0 CRC64;
MDLVLETLDH YIFDDVYAKI APVELQRGID DSLVNALSLN KIVSNSTLLH ETLSITNSLK
RVNKDVYGLT PFLFDFTEKT YASLLPRNNL IREFFSLWAV VTVFGLLLYL ITASLSYVFV
FDRTIFNHPK YLKNQMYLEI KLAVSAIPTM SLLTVPWFML ELNGYSKLYY DVDWEHHGLR
KLLIEYATFI FFTDCGIYLA HRWLHWPRVY KALHKPHHKW LVCTPFASHA FHPVDGYFQS
LSYHIYPMIL PLHKISYLIL FTFVNFWSVM IHDGQHMSNN PVVNGTACHT VHHLYFNYNY
GQFTTLWDRL GGSYRRPEDS LFDPKLKMDK KVLEKQARET AAYIQEVEGD DTDRVYNTDK
KKTN
